Active-learning pedagogies have been repeatedly demonstrated to produce superior learning gains with large effect sizes compared with lecture-based pedagogies. Shifting large numbers of college science, technology, engineering, and mathematics (STEM) faculty to include any active learning in their teaching may retain and more effectively educate far more students than having a few faculty completely transform their teaching, but the extent to which STEM faculty are changing their teaching methods is unclear. Here, we describe the development and application of the machine-learning-derived algorithm Decibel Analysis for Research in Teaching (DART), which can analyze thousands of hours of STEM course audio recordings quickly, with minimal costs, and without need for human observers. DART analyzes the volume and variance of classroom recordings to predict the quantity of time spent on single voice (e.g., lecture), multiple voice (e.g., pair discussion), and no voice (e.g., clicker question thinking) activities. Applying DART to 1,486 recordings of class sessions from 67 courses, a total of 1,720 h of audio, revealed varied patterns of lecture (single voice) and nonlecture activity (multiple and no voice) use. We also found that there was significantly more use of multiple and no voice strategies in courses for STEM majors compared with courses for non-STEM majors, indicating that DART can be used to compare teaching strategies in different types of courses. Therefore, DART has the potential to systematically inventory the presence of active learning with ∼90% accuracy across thousands of courses in diverse settings with minimal effort.active learning | evidence-based teaching | science education | lecture | assessment C urrent college STEM (science, technology, engineering, and mathematics) teaching in the United States continues to be lecture-based and is relatively ineffective in promoting learning (1, 2). Undergraduate instructors continue to struggle to engage, effectively teach, and retain postsecondary students, both generally and particularly among women and students of color (3, 4). Federal analyses suggest that a 10% increase in retention of undergraduate STEM students could address anticipated STEM workforce shortfalls (5). Replacing the standard lecture format with more active teaching strategies has been shown to increase
Machine Learning (ML) methods are now influencing major decisions about patient care, new medical methods, drug development and their use and importance are rapidly increasing in all areas. However, these ML methods are inherently complex and often difficult to understand and explain resulting in barriers to their adoption and validation. Our work (RFEX) focuses on enhancing Random Forest (RF) classifier explainability by developing easy to interpret explainability summary reports from trained RF classifiers as a way to improve the explainability for (often non-expert) users. RFEX is implemented and extensively tested on Stanford FEATURE data where RF is tasked with predicting functional sites in 3D molecules based on their electrochemical signatures (features). In developing RFEX method we apply user-centered approach driven by explainability questions and requirements collected by discussions with interested practitioners. We performed formal usability testing with 13 expert and non-expert users to verify RFEX usefulness. Analysis of RFEX explainability report and user feedback indicates its usefulness in significantly increasing explainability and user confidence in RF classification on FEATURE data. Notably, RFEX summary reports easily reveal that one needs very few (from 2-6 depending on a model) top ranked features to achieve 90% or better of the accuracy when all 480 features are used.
BackgroundWith the emergence of a completed genome sequence of the freshwater crustacean Daphnia pulex, construction of genomic-scale sequence databases for additional crustacean sequences are important for comparative genomics and annotation. Porcelain crabs, genus Petrolisthes, have been powerful crustacean models for environmental and evolutionary physiology with respect to thermal adaptation and understanding responses of marine organisms to climate change. Here, we present a large-scale EST sequencing and cDNA microarray database project for the porcelain crab Petrolisthes cinctipes.Methodology/Principal FindingsA set of ∼30K unique sequences (UniSeqs) representing ∼19K clusters were generated from ∼98K high quality ESTs from a set of tissue specific non-normalized and mixed-tissue normalized cDNA libraries from the porcelain crab Petrolisthes cinctipes. Homology for each UniSeq was assessed using BLAST, InterProScan, GO and KEGG database searches. Approximately 66% of the UniSeqs had homology in at least one of the databases. All EST and UniSeq sequences along with annotation results and coordinated cDNA microarray datasets have been made publicly accessible at the Porcelain Crab Array Database (PCAD), a feature-enriched version of the Stanford and Longhorn Array Databases.Conclusions/SignificanceThe EST project presented here represents the third largest sequencing effort for any crustacean, and the largest effort for any crab species. Our assembly and clustering results suggest that our porcelain crab EST data set is equally diverse to the much larger EST set generated in the Daphnia pulex genome sequencing project, and thus will be an important resource to the Daphnia research community. Our homology results support the pancrustacea hypothesis and suggest that Malacostraca may be ancestral to Branchiopoda and Hexapoda. Our results also suggest that our cDNA microarrays cover as much of the transcriptome as can reasonably be captured in EST library sequencing approaches, and thus represent a rich resource for studies of environmental genomics.
We address the problem of assigning biological function to solved protein structures. Computational tools play a critical role in identifying potential active sites and informing screening decisions for further lab analysis. A critical parameter in the practical application of computational methods is the precision, or positive predictive value. Precision measures the level of confidence the user should have in a particular computed functional assignment. Low precision annotations lead to futile laboratory investigations and waste scarce research resources. In this paper we describe an advanced version of the protein function annotation system FEATURE, which achieved 99% precision and average recall of 95% across 20 representative functional sites. The system uses a Support Vector Machine classifier operating on the microenvironment of physicochemical features around an amino acid. We also compared performance of our method with state-of-the-art sequence-level annotator Pfam in terms of precision, recall and localization. To our knowledge, no other functional site annotator has been rigorously evaluated against these key criteria. The software and predictive models are incorporated into the WebFEATURE service at http://feature.stanford.edu/wf4.0-beta.
Machine learning-based prediction of protein functions plays a key role in bioinformatics and pharmaceutical research, facilitating swift discovery of new drugs in highthroughput settings. This paper presents an adaptation of Random Forest to the structure-based protein function prediction. Our system represents protein's 3D physicochemical structural information in microenvironment descriptors whose spatial resolution is much finer than other sequence-based protein descriptors. We prepare our datasets for seven active sites from five protein function classes by using multiple public data banks and train Random Forest classifiers to identify these seven function models in proteins. This paper presents two experiment studies: 1) a 5-fold stratified cross-validation for comparing Random Forest with Naive Bayes and Support Vector Machine and 2) systematic comparison of Random Forest's two variable importance measures. Promising results of these studies demonstrate a potential for Random Forest to improve the accuracy of the current protein function assays.
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